O08336 · CYPB_BACSU
- ProteinBifunctional cytochrome P450/NADPH--P450 reductase 2
- GenecypB
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1054 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of a range of medium to long-chain fatty acids, with a preference for long-chain unsaturated and branched-chain fatty acids over saturated fatty acids. Hydroxylation of myristic acid occurs mainly at the omega-2 and omega-3 positions, in approximately equal proportions. Also displays a NADPH-dependent reductase activity in the C-terminal domain, which allows electron transfer from NADPH to the heme iron of the cytochrome P450 N-terminal domain.
Catalytic activity
- an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H+ + H2O + oxidized [NADPH--hemoprotein reductase]
Cofactor
Protein has several cofactor binding sites:
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
165 μM | lauric acid | |||||
542 μM | myristic acid | |||||
337 μM | palmitic acid | |||||
68.5 μM | stearic acid | |||||
28.7 μM | phytanic acid | |||||
68.3 μM | 15-methylpalmitic acid | |||||
79 μM | arachidonic acid | |||||
5.1 μM | NADPH | |||||
2.43 mM | NADH | |||||
10.9 μM | cytochrome c | in the reductase assay | ||||
285 μM | ferricyanide | in the reductase assay |
kcat is 104 min-1 for lauric acid hydroxylation. kcat is 5556 min-1 for myristic acid hydroxylation. kcat is 676 min-1 for palmitic acid hydroxylation. kcat is 374 min-1 for stearic acid hydroxylation. kcat is 794 min-1 for phytanic acid hydroxylation. kcat is 3845 min-1 for 15-methylpalmitic acid hydroxylation. kcat is 1690 min-1 for arachidonic acid hydroxylation. kcat is 3520 min-1 for the reduction of cytochrome c. kcat is 37050 min-1 for the reduction of ferricyanide.
Features
Showing features for site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 271 | Important for catalytic activity | ||||
Sequence: T | ||||||
Binding site | 403 | Fe (UniProtKB | ChEBI) of heme (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: C | ||||||
Binding site | 492-497 | FMN (UniProtKB | ChEBI) | ||||
Sequence: SNLGTA | ||||||
Binding site | 539-542 | FMN (UniProtKB | ChEBI) | ||||
Sequence: SYNG | ||||||
Binding site | 573-575 | FMN (UniProtKB | ChEBI) | ||||
Sequence: CGN | ||||||
Binding site | 581-583 | FMN (UniProtKB | ChEBI) | ||||
Sequence: TYQ |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | aromatase activity | |
Molecular Function | fatty acid binding | |
Molecular Function | flavin adenine dinucleotide binding | |
Molecular Function | FMN binding | |
Molecular Function | heme binding | |
Molecular Function | iron ion binding | |
Molecular Function | NADPH-hemoprotein reductase activity | |
Molecular Function | oxidoreductase activity | |
Molecular Function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen | |
Biological Process | fatty acid oxidation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBifunctional cytochrome P450/NADPH--P450 reductase 2
- Alternative names
Including 2 domains:
- Recommended nameCytochrome P450 102A3
- EC number
- Recommended nameNADPH--cytochrome P450 reductase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Bacillus
Accessions
- Primary accessionO08336
Proteomes
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 89 | Hydroxylates shorter substrates with higher conversion rates than wild-type, and in contrast to wild-type, is also able to convert medium-chain alkanes and aromatic compounds; when associated with Q-190. | ||||
Sequence: F → V | ||||||
Mutagenesis | 190 | Hydroxylates shorter substrates with higher conversion rates than wild-type, and in contrast to wild-type, is also able to convert medium-chain alkanes and aromatic compounds; when associated with V-89. | ||||
Sequence: S → Q |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000052207 | 1-1054 | Bifunctional cytochrome P450/NADPH--P450 reductase 2 | |||
Sequence: MKQASAIPQPKTYGPLKNLPHLEKEQLSQSLWRIADELGPIFRFDFPGVSSVFVSGHNLVAEVCDEKRFDKNLGKGLQKVREFGGDGLFTSWTHEPNWQKAHRILLPSFSQKAMKGYHSMMLDIATQLIQKWSRLNPNEEIDVADDMTRLTLDTIGLCGFNYRFNSFYRDSQHPFITSMLRALKEAMNQSKRLGLQDKMMVKTKLQFQKDIEVMNSLVDRMIAERKANPDENIKDLLSLMLYAKDPVTGETLDDENIRYQIITFLIAGHETTSGLLSFAIYCLLTHPEKLKKAQEEADRVLTDDTPEYKQIQQLKYIRMVLNETLRLYPTAPAFSLYAKEDTVLGGEYPISKGQPVTVLIPKLHRDQNAWGPDAEDFRPERFEDPSSIPHHAYKPFGNGQRACIGMQFALQEATMVLGLVLKHFELINHTGYELKIKEALTIKPDDFKITVKPRKTAAINVQRKEQADIKAETKPKETKPKHGTPLLVLFGSNLGTAEGIAGELAAQGRQMGFTAETAPLDDYIGKLPEEGAVVIVTASYNGAPPDNAAGFVEWLKELEEGQLKGVSYAVFGCGNRSWASTYQRIPRLIDDMMKAKGASRLTAIGEGDAADDFESHRESWENRFWKETMDAFDINEIAQKEDRPSLSITFLSEATETPVAKAYGAFEGIVLENRELQTAASTRSTRHIELEIPAGKTYKEGDHIGILPKNSRELVQRVLSRFGLQSNHVIKVSGSAHMAHLPMDRPIKVVDLLSSYVELQEPASRLQLRELASYTVCPPHQKELEQLVSDDGIYKEQVLAKRLTMLDFLEDYPACEMPFERFLALLPSLKPRYYSISSSPKVHANIVSMTVGVVKASAWSGRGEYRGVASNYLAELNTGDAAACFIRTPQSGFQMPNDPETPMIMVGPGTGIAPFRGFIQARSVLKKEGSTLGEALLYFGCRRPDHDDLYREELDQAEQDGLVTIRRCYSRVENEPKGYVQHLLKQDTQKLMTLIEKGAHIYVCGDGSQMAPDVERTLRLAYEAEKAASQEESAVWLQKLQDQRRYVKDVWTGM |
Proteomic databases
Expression
Induction
Negatively regulated by the transcriptional repressor FatR (PubMed:11574077, PubMed:11734890).
Is induced by fatty acids such as oleate, linoleate and phytanate, that bind and displace the FatR repressor (PubMed:11734890).
Is also induced by palmitate, likely via another mechanism (PubMed:11574077).
Transcribed under partial control of SigM ECF sigma factor (PubMed:17434969).
Is induced by fatty acids such as oleate, linoleate and phytanate, that bind and displace the FatR repressor (PubMed:11734890).
Is also induced by palmitate, likely via another mechanism (PubMed:11574077).
Transcribed under partial control of SigM ECF sigma factor (PubMed:17434969).
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-475 | Cytochrome P450 | ||||
Sequence: MKQASAIPQPKTYGPLKNLPHLEKEQLSQSLWRIADELGPIFRFDFPGVSSVFVSGHNLVAEVCDEKRFDKNLGKGLQKVREFGGDGLFTSWTHEPNWQKAHRILLPSFSQKAMKGYHSMMLDIATQLIQKWSRLNPNEEIDVADDMTRLTLDTIGLCGFNYRFNSFYRDSQHPFITSMLRALKEAMNQSKRLGLQDKMMVKTKLQFQKDIEVMNSLVDRMIAERKANPDENIKDLLSLMLYAKDPVTGETLDDENIRYQIITFLIAGHETTSGLLSFAIYCLLTHPEKLKKAQEEADRVLTDDTPEYKQIQQLKYIRMVLNETLRLYPTAPAFSLYAKEDTVLGGEYPISKGQPVTVLIPKLHRDQNAWGPDAEDFRPERFEDPSSIPHHAYKPFGNGQRACIGMQFALQEATMVLGLVLKHFELINHTGYELKIKEALTIKPDDFKITVKPRKTAAINVQRKEQADIKAETKP | ||||||
Compositional bias | 462-481 | Basic and acidic residues | ||||
Sequence: QRKEQADIKAETKPKETKPK | ||||||
Region | 462-482 | Disordered | ||||
Sequence: QRKEQADIKAETKPKETKPKH | ||||||
Region | 476-1053 | NADPH--P450 reductase | ||||
Sequence: KETKPKHGTPLLVLFGSNLGTAEGIAGELAAQGRQMGFTAETAPLDDYIGKLPEEGAVVIVTASYNGAPPDNAAGFVEWLKELEEGQLKGVSYAVFGCGNRSWASTYQRIPRLIDDMMKAKGASRLTAIGEGDAADDFESHRESWENRFWKETMDAFDINEIAQKEDRPSLSITFLSEATETPVAKAYGAFEGIVLENRELQTAASTRSTRHIELEIPAGKTYKEGDHIGILPKNSRELVQRVLSRFGLQSNHVIKVSGSAHMAHLPMDRPIKVVDLLSSYVELQEPASRLQLRELASYTVCPPHQKELEQLVSDDGIYKEQVLAKRLTMLDFLEDYPACEMPFERFLALLPSLKPRYYSISSSPKVHANIVSMTVGVVKASAWSGRGEYRGVASNYLAELNTGDAAACFIRTPQSGFQMPNDPETPMIMVGPGTGIAPFRGFIQARSVLKKEGSTLGEALLYFGCRRPDHDDLYREELDQAEQDGLVTIRRCYSRVENEPKGYVQHLLKQDTQKLMTLIEKGAHIYVCGDGSQMAPDVERTLRLAYEAEKAASQEESAVWLQKLQDQRRYVKDVWTG | ||||||
Domain | 486-625 | Flavodoxin-like | ||||
Sequence: LLVLFGSNLGTAEGIAGELAAQGRQMGFTAETAPLDDYIGKLPEEGAVVIVTASYNGAPPDNAAGFVEWLKELEEGQLKGVSYAVFGCGNRSWASTYQRIPRLIDDMMKAKGASRLTAIGEGDAADDFESHRESWENRFW | ||||||
Domain | 663-896 | FAD-binding FR-type | ||||
Sequence: YGAFEGIVLENRELQTAASTRSTRHIELEIPAGKTYKEGDHIGILPKNSRELVQRVLSRFGLQSNHVIKVSGSAHMAHLPMDRPIKVVDLLSSYVELQEPASRLQLRELASYTVCPPHQKELEQLVSDDGIYKEQVLAKRLTMLDFLEDYPACEMPFERFLALLPSLKPRYYSISSSPKVHANIVSMTVGVVKASAWSGRGEYRGVASNYLAELNTGDAAACFIRTPQSGFQMP |
Sequence similarities
In the N-terminal section; belongs to the cytochrome P450 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,054
- Mass (Da)118,676
- Last updated1997-07-01 v1
- Checksum705F8E27866CA110
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 462-481 | Basic and acidic residues | ||||
Sequence: QRKEQADIKAETKPKETKPK |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U93874 EMBL· GenBank· DDBJ | AAB80867.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL009126 EMBL· GenBank· DDBJ | CAB14658.1 EMBL· GenBank· DDBJ | Genomic DNA |